Peroxidative catalytic behavior of cytochrome c solubilized in reverse micelles

Tsutomu Ono, Masahiro Goto

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)


Solubilization of horse heart cytochrome c into reverse micelles, a self-assembled nanostructure composed of sodium di-2-ethylhexyl sulfosuccinate (AOT), enhances the peroxidase activity in the presence of hydrogen peroxide. The catalytic activity of cytochrome c hosted in reverse micellar solution is 10-fold higher than that in water, and which depends on Wo, a molar ratio of water to AOT, and pH in aqueous droplets. In addition, the fluorescence intensity based on the tryptophan residue and the visible absorption identifying the axial Met 80-Fe bond imply that the reverse micellar solubilization induces the cleavage of the heme crevice and thus enables the formation of peroxidase-like peroxide-heme complexes. These results suggest that cytochrome c solubilized in reverse micelles provides a homogeneous catalyst as peroxidase available in organic media.

Original languageEnglish
Pages (from-to)156-160
Number of pages5
JournalBiochemical Engineering Journal
Issue number2
Publication statusPublished - Feb 15 2006
Externally publishedYes


  • Microemulsion
  • Oxidation
  • Peroxidase
  • Surfactant

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Environmental Engineering
  • Biomedical Engineering


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